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Related Experiment Videos

The cell attachment determinant in fibronectin.

M D Pierschbacher, E G Hayman, E Ruoslahti

    Journal of Cellular Biochemistry
    |January 1, 1985
    PubMed
    Summary
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    A short amino acid sequence, glycyl-L-arginyl-glycyl-L-aspartyl-L-serine, mimics fibronectin's cell attachment ability. This Arg-Gly-Asp sequence is a key cellular recognition mechanism found in many proteins.

    Area of Science:

    • Biochemistry
    • Cell Biology
    • Molecular Biology

    Background:

    • Fibronectin is a protein that mediates cell adhesion through a specific domain.
    • The cell-binding function of fibronectin can be replicated by a short peptide sequence.

    Purpose of the Study:

    • To identify and characterize the minimal amino acid sequence responsible for fibronectin-mediated cell attachment.
    • To investigate the prevalence and significance of this recognition sequence in other cell-interactive proteins.

    Main Methods:

    • Peptide synthesis and functional assays to test cell attachment.
    • Bioinformatic analysis to identify similar sequences in other proteins.

    Main Results:

    • The peptide glycyl-L-arginyl-glycyl-L-aspartyl-L-serine effectively promotes cell attachment.

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  • The Arg-Gly-Asp tripeptide is crucial for activity, while serine can be substituted with limitations.
  • Similar Arg-Gly-Asp-like sequences are found in various proteins, including collagens, fibrinogen, and viral proteins.

    • Conclusions:

    • The Arg-Gly-Asp sequence represents a fundamental cell recognition motif.
    • This motif may be an ancient and widespread mechanism for protein-cell interactions across diverse species and protein types.